WNT5A_PLEWA
ID WNT5A_PLEWA Reviewed; 359 AA.
AC O13267;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Protein Wnt-5a;
DE Short=PWnt-5a;
DE Flags: Precursor;
GN Name=WNT5A;
OS Pleurodeles waltl (Iberian ribbed newt).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Caudata; Salamandroidea; Salamandridae; Pleurodelinae;
OC Pleurodeles.
OX NCBI_TaxID=8319;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9286590;
RX DOI=10.1002/(sici)1097-0177(199709)210:1<1::aid-aja1>3.0.co;2-l;
RA Caubit X., Nicolas S., Le Parco Y.;
RT "Possible roles for Wnt genes in growth and axial patterning during
RT regeneration of the tail in urodele amphibians.";
RL Dev. Dyn. 210:1-10(1997).
CC -!- FUNCTION: Ligand for members of the frizzled family of seven
CC transmembrane receptors. Can activate or inhibit canonical Wnt
CC signaling, depending on receptor context. Required during embryogenesis
CC for extension of the primary anterior-posterior axis.
CC {ECO:0000250|UniProtKB:P22725}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250|UniProtKB:P41221}. Secreted
CC {ECO:0000250|UniProtKB:P41221}.
CC -!- PTM: Palmitoleoylation is required for efficient binding to frizzled
CC receptors. Depalmitoleoylation leads to Wnt signaling pathway
CC inhibition. {ECO:0000250|UniProtKB:P27467,
CC ECO:0000250|UniProtKB:P56704}.
CC -!- SIMILARITY: Belongs to the Wnt family. {ECO:0000305}.
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DR EMBL; U80582; AAB58495.1; -; Genomic_DNA.
DR AlphaFoldDB; O13267; -.
DR SMR; O13267; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 3.30.2460.20; -; 1.
DR InterPro; IPR005817; Wnt.
DR InterPro; IPR026538; Wnt5a.
DR InterPro; IPR043158; Wnt_C.
DR InterPro; IPR018161; Wnt_CS.
DR PANTHER; PTHR12027; PTHR12027; 1.
DR PANTHER; PTHR12027:SF33; PTHR12027:SF33; 1.
DR Pfam; PF00110; wnt; 1.
DR PRINTS; PR01349; WNTPROTEIN.
DR SMART; SM00097; WNT1; 1.
DR PROSITE; PS00246; WNT1; 1.
PE 3: Inferred from homology;
KW Developmental protein; Disulfide bond; Extracellular matrix; Glycoprotein;
KW Lipoprotein; Secreted; Signal; Wnt signaling pathway.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..359
FT /note="Protein Wnt-5a"
FT /id="PRO_0000041430"
FT LIPID 223
FT /note="O-palmitoleoyl serine; by PORCN"
FT /evidence="ECO:0000250|UniProtKB:P56704"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 305
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 83..94
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 133..141
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 143..161
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 217..231
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 219..226
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 288..319
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 304..314
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 318..358
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 334..349
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 336..346
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 341..342
FT /evidence="ECO:0000250|UniProtKB:P28026"
SQ SEQUENCE 359 AA; 40346 MW; 425CF9C6614137FB CRC64;
MASRYLTLAA ALLASFLQVD IEANSWWSLA MNPVQIPEAY IVGAQPLCSQ LAGLSPGQKK
LCQLYQDHMQ YIGEGAKTGI KECQYQFRHR RWNCSTVDNI SVFGRVMQIG SRETAFTYSI
SAAGVVNAVS RACRAGELST CGCSRARRPK DLQRDWLWGG CGDNLDYGYR FAKEFVDARE
REKIHQKGSY ESSRTLMNLH NNEAGRRTVY NLADVACKCH GVSGSCSLKT CWLQLADFRK
VGDFLKEKYD SAASMKLNSR GKLVQVNSRF NPPTTNDLVY VDPSPDYCVR NESTGSMGTQ
GRLCNKTSEG MDGCELMCCG RGYDQFKTVQ TERCHCKFHW CCYVKCKKCT EIVDQFVCK